Sentence examples for binding equation was used from inspiring English sources

A one-site binding equation was used to determine the values for maximal binding (Bmax) and the equilibrium dissociation constants (Kd) with n denoting the number of independent experiments (SN: Kd = 1.09 nM±0.05, n = 6; NiE: Kd = 0.41 nM±0.03, n = 6; NTE: Kd = 0.46 nM±0.05, n = 4).

A ligand-depleted binding equation was used to fit the fluorescent quenching data (Equation 1).

To further elucidate the binding constants (Ka) and the number of binding sites (n), the modified Stern Volmer equation was used [37]: { lg }left[ {left( {{text{F}}_{0} - {text{ F}}} right)/{text{F}}} right] = {text{ lg K}}_{text{a}} + {text{ n lg }}left[ {text{Q}} right]where Ka and n represent the binding constant and the number of binding sites, respectively.

To calculate binding affinity of a test set in pKi, following equation was used in DS: pKi = A+(B vdW) + (C c+pol)−(D BuryPol2).

For the exposure estimation, simple, first-tier equations were used.

One of these equations is used for transverse magnetic (TM) modes to introduce an eigenvalue-eigenfunction equation of the PC slab in tight binding method.

b Generalized Estimating Equations are used.

The integrated rate equation for stoichiometric binding was used to calculate association rate constants (Table 2).

The equation for non-linear one site binding (hyperbola) Y = Bmax*X/ Kd+X) was used to calculate Kd and Bmax values using Graphpad software.

The resulting equation (eq 6) (procedures of the Supporting Information) was used to globally fit this binding model where n is the number of identical sites (three).

The MM-PB/SA was employed for calculating the free energy of binding and the equation described by Okimoto et al [ 37] was used.